OAZ1

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Ornithine decarboxylase antizyme 1
Identifiers
Symbol(s) OAZ1; AZI; MGC138338; OAZ
External IDs OMIM: 601579 MGI: 109433 HomoloGene: 7455
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 4946 18245
Ensembl ENSG00000104904 ENSMUSG00000035242
Uniprot P54368 Q52KL6
Refseq NM_004152 (mRNA)
NP_004143 (protein)		 NM_008753 (mRNA)
NP_032779 (protein)
Location Chr 19: 2.22 - 2.22 Mb Chr 10: 80.23 - 80.23 Mb
Pubmed search [1] [2]

Ornithine decarboxylase antizyme 1, also known as OAZ1, is a human gene.[1]

Ornithine decarboxylase catalyzes the conversion of ornithine to putrescine in the first and apparently rate-limiting step in polyamine biosynthesis. The ornithine decarboxylase antizymes play a role in the regulation of polyamine synthesis by binding to and inhibiting ornithine decarboxylase. Antizyme expression is auto-regulated by polyamine-enhanced translational frameshifting. The antizyme encoded by this gene inhibits ornithine decarboxylase and accelerates its degradation.[1]

[edit] References

  1. ^ a b Entrez Gene: OAZ1 ornithine decarboxylase antizyme 1.

[edit] Further reading

  • Coffino P (2000). "Polyamines in spermiogenesis: not now, darling.". Proc. Natl. Acad. Sci. U.S.A. 97 (9): 4421-3. PMID 10781034. 
  • Savage RE, Nofzinger K, Bedell C, et al. (1989). "Chloroform-induced multiple forms of ornithine decarboxylase: differential sensitivity of forms to enhancement by diethyl maleate and inhibition by ODC-antizyme.". Journal of toxicology and environmental health 27 (1): 57-64. PMID 2724368. 
  • Tewari DS, Qian Y, Thornton RD, et al. (1995). "Molecular cloning and sequencing of a human cDNA encoding ornithine decarboxylase antizyme.". Biochim. Biophys. Acta 1209 (2): 293-5. PMID 7811704. 
  • Matsufuji S, Matsufuji T, Miyazaki Y, et al. (1995). "Autoregulatory frameshifting in decoding mammalian ornithine decarboxylase antizyme.". Cell 80 (1): 51-60. PMID 7813017. 
  • Mamroud-Kidron E, Omer-Itsicovich M, Bercovich Z, et al. (1995). "A unified pathway for the degradation of ornithine decarboxylase in reticulocyte lysate requires interaction with the polyamine-induced protein, ornithine decarboxylase antizyme.". Eur. J. Biochem. 226 (2): 547-54. PMID 8001569. 
  • Ichiba T, Matsufuji S, Miyazaki Y, et al. (1994). "Functional regions of ornithine decarboxylase antizyme.". Biochem. Biophys. Res. Commun. 200 (3): 1721-7. doi:10.1006/bbrc.1994.1651. PMID 8185631. 
  • Matsufuji S, Inazawa J, Hayashi T, et al. (1997). "Assignment of the human antizyme gene (OAZ) to chromosome 19p13.3 by fluorescence in situ hybridization.". Genomics 38 (1): 102-4. PMID 8954789. 
  • Yang D, Takii T, Hayashi H, et al. (1997). "Molcecular cloning of human antizyme cDNA.". Biochem. Mol. Biol. Int. 38 (5): 957-64. PMID 9132164. 
  • Hayashi T, Matsufuji S, Hayashi S (1998). "Characterization of the human antizyme gene.". Gene 203 (2): 131-9. PMID 9426243. 
  • Zhu C, Lang DW, Coffino P (1999). "Antizyme2 is a negative regulator of ornithine decarboxylase and polyamine transport.". J. Biol. Chem. 274 (37): 26425-30. PMID 10473601. 
  • Chen H, MacDonald A, Coffino P (2003). "Structural elements of antizymes 1 and 2 are required for proteasomal degradation of ornithine decarboxylase.". J. Biol. Chem. 277 (48): 45957-61. doi:10.1074/jbc.M206799200. PMID 12359729. 
  • Ike A, Yamada S, Tanaka H, et al. (2003). "Structure and promoter activity of the gene encoding ornithine decarboxylase antizyme expressed exclusively in haploid germ cells in testis (OAZt/Oaz3).". Gene 298 (2): 183-93. PMID 12426106. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Grimwood J, Gordon LA, Olsen A, et al. (2004). "The DNA sequence and biology of human chromosome 19.". Nature 428 (6982): 529-35. doi:10.1038/nature02399. PMID 15057824. 
  • Mangold U, Leberer E (2005). "Regulation of all members of the antizyme family by antizyme inhibitor.". Biochem. J. 385 (Pt 1): 21-8. doi:10.1042/BJ20040547. PMID 15355308. 
  • Choi KS, Suh YH, Kim WH, et al. (2005). "Stable siRNA-mediated silencing of antizyme inhibitor: regulation of ornithine decarboxylase activity.". Biochem. Biophys. Res. Commun. 328 (1): 206-12. doi:10.1016/j.bbrc.2004.11.172. PMID 15670771. 
  • Ku M, Howard S, Ni W, et al. (2006). "OAZ regulates bone morphogenetic protein signaling through Smad6 activation.". J. Biol. Chem. 281 (8): 5277-87. doi:10.1074/jbc.M510004200. PMID 16373339. 
  • Lim J, Hao T, Shaw C, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration.". Cell 125 (4): 801-14. doi:10.1016/j.cell.2006.03.032. PMID 16713569. 
  • Tsuji T, Katsurano M, Ibaragi S, et al. (2007). "Ornithine decarboxylase antizyme upregulates DNA-dependent protein kinase and enhances the nonhomologous end-joining repair of DNA double-strand breaks in human oral cancer cells.". Biochemistry 46 (31): 8920-32. doi:10.1021/bi7000328. PMID 17630775. 
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